Mass conserved elementary kinetics is sufficient for the existence of a non-equilibrium steady state concentration

TL;DR

This paper establishes that mass conservation in elementary kinetics ensures the existence of non-equilibrium steady states in biochemical networks, providing a general, verifiable framework for modeling forced non-equilibrium conditions.

Contribution

It introduces a general formulation for forcing large kinetic models to maintain non-equilibrium steady states based solely on mass balance and positive concentrations.

Findings

Mass conservation guarantees steady state existence.

Conditions for forcing systems are polynomial-time verifiable.

Example demonstrates perpetual forcing with infeasible parameters.

Abstract

Living systems are forced away from thermodynamic equilibrium by exchange of mass and energy with their environment. In order to model a biochemical reaction network in a non-equilibrium state one requires a mathematical formulation to mimic this forcing. We provide a general formulation to force an arbitrary large kinetic model in a manner that is still consistent with the existence of a non-equilibrium steady state. We can guarantee the existence of a non-equilibrium steady state assuming only two conditions; that every reaction is mass balanced and that continuous kinetic reaction rate laws never lead to a negative molecule concentration. These conditions can be verified in polynomial time and are flexible enough to permit one to force a system away from equilibrium. In an expository biochemical example we show how a reversible, mass balanced perpetual reaction, with thermodynamically infeasible kinetic parameters, can be used to perpetually force a kinetic model of anaerobic glycolysis in a manner consistent with the existence of a steady state. Easily testable existence conditions are foundational for efforts to reliably compute non-equilibrium steady states in genome-scale biochemical kinetic models.